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Article

ALS-causing hPFN1 mutants differentially disrupt LLPS of FUS prion-like domain.

Biochemical and biophysical research communications - 5 Jul 2023

Kang Jian, Lim Liangzhong, Song Jianxing

Abstract excerpt

hPFN1 mutations including C71G cause ALS by gain of toxicity but the mechanism still remains unknown. Stress granules (SGs) are formed by phase separation of the prion-like domain (PLD) of RNA-binding proteins including FUS, whose inclusion was also associated with ALS. C71G-hPFN1 triggers seed-dependent co-aggregation with FUS/TDP-43 to manifest the prion-like propagandation but its biophysical basis remains...

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PMID: 37130459
DOI: 10.1016/j.bbrc.2023.04.101

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